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-Structure paper
タイトル | Structural basis of Q-dependent transcription antitermination. |
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ジャーナル・号・ページ | Nat Commun, Vol. 10, Issue 1, Page 2925, Year 2019 |
掲載日 | 2019年7月2日 |
著者 | Jing Shi / Xiang Gao / Tongguan Tian / Zhaoyang Yu / Bo Gao / Aijia Wen / Linlin You / Shenghai Chang / Xing Zhang / Yu Zhang / Yu Feng / |
PubMed 要旨 | Bacteriophage Q protein engages σ-dependent paused RNA polymerase (RNAP) by binding to a DNA site embedded in late gene promoter and renders RNAP resistant to termination signals. Here, we report a ...Bacteriophage Q protein engages σ-dependent paused RNA polymerase (RNAP) by binding to a DNA site embedded in late gene promoter and renders RNAP resistant to termination signals. Here, we report a single-particle cryo-electron microscopy (cryo-EM) structure of an intact Q-engaged arrested complex. The structure reveals key interactions responsible for σ-dependent pause, Q engagement, and Q-mediated transcription antitermination. The structure shows that two Q protomers (Q and Q) bind to a direct-repeat DNA site and contact distinct elements of the RNA exit channel. Notably, Q forms a narrow ring inside the RNA exit channel and renders RNAP resistant to termination signals by prohibiting RNA hairpin formation in the RNA exit channel. Because the RNA exit channel is conserved among all multisubunit RNAPs, it is likely to serve as an important contact site for regulators that modify the elongation properties of RNAP in other organisms, as well. |
リンク | Nat Commun / PubMed:31266960 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 1.451 - 4.08 Å |
構造データ | PDB-6jny: |
化合物 | ChemComp-MG: ChemComp-ZN: ChemComp-HOH: |
由来 |
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キーワード | TRANSCRIPTION / DNA / RNA / RNA polymerase / Antitermination |